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Structure of PDB 1gwv Chain B

Receptor sequence >1gwvB (length=287) Species: 9913 (Bos taurus) [Search protein sequence] KLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGL TVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPL RSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQ DKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHA AIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHLNKYFLLNKPTK ILSPEYCWDYHIGLPADIKLVKMSWQTKEYNVVRNNV

3D structure PDB 1gwv Structural Basis of Ordered Binding of Donor and Acceptor Substrates to the Retaining Glycosyltransferase, Alpha -1,3 Galactosyltransferase Chain B Resolution 2.5 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) Q247 H280 W314 E317 W356 R365 Catalytic site (residue number reindexed from 1) Q166 H199 W233 E236 W275 R284 Enzyme Commision number 2.4.1.87: N-acetyllactosaminide 3-alpha-galactosyltransferase.

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 BGC B W249 W250 W168 W169 BS02 GAL B Q247 T259 W314 E317 W356 K359 Q166 T178 W233 E236 W275 K278 BS03 UDP B F134 A135 V136 Y139 I198 R202 D225 V226 D227 K359 Y361 R365 F53 A54 V55 Y58 I117 R121 D144 V145 D146 K278 Y280 R284 MOAD: Kd=0.053mM BS04 MN B D225 D227 D144 D146

Gene Ontology Molecular Function GO:0016758 hexosyltransferase activity

	Biological Process
GO:0005975	carbohydrate metabolic process

	Cellular Component
GO:0016020	membrane

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